Pseudolysin (LasB)

Pseudolysin, commonly referred to as LasB elastase, is a potent extracellular zinc metalloprotease and a primary virulence factor secreted by the opportunistic pathogen Pseudomonas aeruginosa [1, 9]. It plays a multifaceted role in infection by degrading a wide range of host proteins, including elastin, collagen, and laminin, which leads to extensive tissue damage and facilitates bacterial invasion [5, 7, 15]. Beyond structural degradation, LasB subverts the host immune system by cleaving immunoglobulins, complement components, and various cytokines, thereby promoting immune evasion and persistent colonization [3, 7, 8]. It is also implicated in the regulation of biofilm formation and the activation of other bacterial enzymes [1, 14]. Because LasB is secreted into the extracellular environment, it is an accessible therapeutic target that does not require drugs to penetrate the complex Gram-negative bacterial cell wall [2, 6]. Current drug development efforts focus on pathoblockers—small-molecule inhibitors like phosphonates and thiols—that aim to attenuate virulence and enhance the efficacy of conventional antibiotics without inducing the selective pressure associated with traditional bactericidal agents [1, 2, 4].

Other names

LasB elastaseElastase BPseudomonas aeruginosa elastasePseudomonas elastaseZinc metalloendopeptidase

Inhibition of the zinc-dependent catalytic site of the metalloprotease to prevent the degradation of host tissues and immune components [1, 2, 5].